Crystallization and preliminary crystallographic analysis of the human calcineurin homologous protein CHP2 bound to the cytoplasmic region of the Na+/H+ exchanger NHE1
Crystallization and preliminary crystallographic analysis of the human calcineurin homologous protein CHP2 bound to the cytoplasmic region of the Na+/H+ exchanger NHE1
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DOI：
10.1107/s1744309105030836
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发表时间：
2005-10-01
影响因子：
0.9
通讯作者：
Wakabayashi, S
中科院分区：
文献类型：
--
作者：
Ben Ammar, Y;Takeda, S;Wakabayashi, S
钙调神经磷酸酶同源蛋白(CHP)是一种钙离子结合蛋白，直接与质膜Na+/H+交换器(NHE)家族成员相互作用并调节其活性。与普遍存在的CHP1亚型不同，CHP2在癌细胞中高表达。为了解CHP2对NHE1的调控机制，以聚乙二醇3350为沉淀剂，采用坐滴气相扩散法结晶了CHP2-NHE1(氨基酸503-545)。晶体衍射角为2.7埃，属四方空间群，晶胞参数a=b=49.96，c=103.20埃。
Calcineurin homologous protein (CHP) is a Ca2+ -binding protein that directly interacts with and regulates the activity of all plasma-membrane Na+/H+ -exchanger (NHE) family members. In contrast to the ubiquitous isoform CHP1, CHP2 is highly expressed in cancer cells. To understand the regulatory mechanism of NHE1 by CHP2, the complex CHP2-NHE1 (amino acids 503-545) has been crystallized by the sitting-drop vapour-diffusion method using PEG 3350 as precipitant. The crystals diffract to 2.7 angstrom and belong to a tetragonal space group, with unit-cell parameters a = b = 49.96, c = 103.20 angstrom.